TY - JOUR
T1 - Molecular details on multiple cofactor containing redox metalloproteins revealed by infrared and resonance raman spectroscopies
AU - Silveira, Célia M.
AU - Zuccarello, Lidia
AU - Barbosa, Catarina
AU - Caserta, Giorgio
AU - Zebger, Ingo
AU - Hildebrandt, Peter
AU - Todorovic, Smilja
N1 - Funding Information:
Funding: This research was funded by FEDER funds through COMPETE2020—Programa Opera-cional Competitividade e Internacionalização (POCI) and by national funds through FCT—Fundacão para a Ciência e a Tecnologia, grant Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular). S.T. acknowledges grant PTDC/BTM-SAL/29507/2017, C.M.S. acknowledges grant PTDC/BIA-BFS/31026/2017 project, and C.B. acknowledges fellowship 2020.05017.BD all funded by FCT. G.C., I.Z., and P.H. are grateful for funding from the Einstein Foundation Berlin (grant number EVF-2016-277). This work was also supported through the cluster of excellence “UniSysCat“ funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy-EXC2008/1-390540038 and the SPP 1927 ”Iron Sulfur for Life”—ZE 510/2-2 (IZ). The APC was funded by the TIMB3 project, European Union’s Horizon 2020 research and innovation program, under grant agreement No 810856.
Funding Information:
This research was funded by FEDER funds through COMPETE2020?Programa Opera-cional Competitividade e Internacionaliza??o (POCI) and by national funds through FCT?Fundac?o para a Ci?ncia e a Tecnologia, grant Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular). S.T. acknowledges grant PTDC/BTM-SAL/29507/2017, C.M.S. acknowledges grant PTDC/BIA-BFS/31026/2017 project, and C.B. acknowledges fellowship 2020.05017.BD all funded by FCT. G.C., I.Z., and P.H. are grateful for funding from the Einstein Foundation Berlin (grant number EVF-2016-277). This work was also supported through the cluster of excellence ?UniSysCat? funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Founda-tion) under Germany?s Excellence Strategy-EXC2008/1-390540038 and the SPP 1927 ?Iron Sulfur for Life??ZE 510/2-2 (IZ). The APC was funded by the TIMB3 project, European Union?s Horizon 2020 research and innovation program, under grant agreement No 810856.
Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2021/8/2
Y1 - 2021/8/2
N2 - Vibrational spectroscopy and in particular, resonance Raman (RR) spectroscopy, can provide molecular details on metalloproteins containing multiple cofactors, which are often challenging for other spectroscopies. Due to distinct spectroscopic fingerprints, RR spectroscopy has a unique capacity to monitor simultaneously and independently different metal cofactors that can have particular roles in metalloproteins. These include e.g., (i) different types of hemes, for instance hemes c, a and a3 in caa3-type oxygen reductases, (ii) distinct spin populations, such as electron transfer (ET) low-spin (LS) and catalytic high-spin (HS) hemes in nitrite reductases, (iii) different types of Fe-S clusters, such as 3Fe-4S and 4Fe-4S centers in di-cluster ferredoxins, and (iv) bi-metallic center and ET Fe-S clusters in hydrogenases. IR spectroscopy can provide unmatched molecular details on specific enzymes like hydrogenases that possess catalytic centers coordinated by CO and CN− ligands, which exhibit spectrally well separated IR bands. This article reviews the work on metalloproteins for which vibrational spectroscopy has ensured advances in understanding structural and mechanistic properties, including multiple heme-containing proteins, such as nitrite reductases that house a notable total of 28 hemes in a functional unit, respiratory chain complexes, and hydrogenases that carry out the most fundamental functions in cells.
AB - Vibrational spectroscopy and in particular, resonance Raman (RR) spectroscopy, can provide molecular details on metalloproteins containing multiple cofactors, which are often challenging for other spectroscopies. Due to distinct spectroscopic fingerprints, RR spectroscopy has a unique capacity to monitor simultaneously and independently different metal cofactors that can have particular roles in metalloproteins. These include e.g., (i) different types of hemes, for instance hemes c, a and a3 in caa3-type oxygen reductases, (ii) distinct spin populations, such as electron transfer (ET) low-spin (LS) and catalytic high-spin (HS) hemes in nitrite reductases, (iii) different types of Fe-S clusters, such as 3Fe-4S and 4Fe-4S centers in di-cluster ferredoxins, and (iv) bi-metallic center and ET Fe-S clusters in hydrogenases. IR spectroscopy can provide unmatched molecular details on specific enzymes like hydrogenases that possess catalytic centers coordinated by CO and CN− ligands, which exhibit spectrally well separated IR bands. This article reviews the work on metalloproteins for which vibrational spectroscopy has ensured advances in understanding structural and mechanistic properties, including multiple heme-containing proteins, such as nitrite reductases that house a notable total of 28 hemes in a functional unit, respiratory chain complexes, and hydrogenases that carry out the most fundamental functions in cells.
KW - Fe-S clusters
KW - Heme proteins
KW - Hydrogenases
KW - IR
KW - Metalloproteins
KW - Resonance Raman spectroscopy
KW - Vibrational spectroscopy
UR - http://www.scopus.com/inward/record.url?scp=85112698979&partnerID=8YFLogxK
U2 - 10.3390/molecules26164852
DO - 10.3390/molecules26164852
M3 - Article
C2 - 34443440
AN - SCOPUS:85112698979
SN - 1420-3049
VL - 26
JO - Molecules
JF - Molecules
IS - 16
M1 - 4852
ER -